996 resultados para Story, Joseph, 1779-1845.
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Tese de doutoramento, História e Filosofia das Ciências, Universidade de Lisboa, Faculdade de Ciências, 2015
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VITAE was a four-year research project designed to explore the work and lives of a purposive sample of 300 Key Stage 1, 2 and 3 (English and maths) teachers at different phases of their careers in 100 primary and secondary schools in different socioeconomic contexts, drawn from seven local authorities in England. Its focus was upon identifying variations in different aspects of teachers' lives and work and examining possible connections between these and their effects on pupils as perceived by the teachers themselves and as measured by value-added national test scores. An integrated mixed-method approach was developed in addressing the research questions. The results showed that there were associations between teachers' work, lives and identities, that teachers' perceived and relative (valueadded) effectiveness varied within each of six professional life phases, and that this variation depended upon their capacity to manage a number of moderating and mediating factors. Statistically significant relationships were found between teacher commitment, resilience and the value-added pupil test scores. The findings from the study shed new light upon the meanings and measurement of teacher effectiveness and the complex nature and trajectories of teachers' work, lives and effectiveness in different school contexts.
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Dissertação de Mestrado, Ciências Biomédicas, 3 de Fevereiro de 2016, Universidade dos Açores.
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Trabalho de projeto apresentado à Escola Superior de Comunicação Social como parte dos requisitos para obtenção de grau de mestre em Audiovisual e Multimédia.
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Stress, molecular crowding and mutations may jeopardize the native folding of proteins. Misfolded and aggregated proteins not only loose their biological activity, but may also disturb protein homeostasis, damage membranes and induce apoptosis. Here, we review the role of molecular chaperones as a network of cellular defenses against the formation of cytotoxic protein aggregates. Chaperones favour the native folding of proteins either as "holdases", sequestering hydrophobic regions in misfolding polypeptides, and/or as "unfoldases", forcibly unfolding and disentangling misfolded polypeptides from aggregates. Whereas in bacteria, plants and fungi Hsp70/40 acts in concert with the Hsp100 (ClpB) unfoldase, Hsp70/40 is the only known chaperone in the cytoplasm of mammalian cells that can forcibly unfold and neutralize cytotoxic protein conformers. Owing to its particular spatial configuration, the bulky 70 kDa Hsp70 molecule, when distally bound through a very tight molecular clamp onto a 50-fold smaller hydrophobic peptide loop extruding from an aggregate, can locally exert on the misfolded segment an unfolding force of entropic origin, thus destroying the misfolded structures that stabilize aggregates. ADP/ATP exchange triggers Hsp70 dissociation from the ensuing enlarged unfolded peptide loop, which is then allowed to spontaneously refold into a closer-to-native conformation devoid of affinity for the chaperone. Driven by ATP, the cooperative action of Hsp70 and its co-chaperone Hsp40 may thus gradually convert toxic misfolded protein substrates with high affinity for the chaperone, into non-toxic, natively refolded, low-affinity products. Stress- and mutation-induced protein damages in the cell, causing degenerative diseases and aging, may thus be effectively counteracted by a powerful network of molecular chaperones and of chaperone-related proteases.
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[Acte royal. 1661-03-16. Paris]
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Référence bibliographique : Rol, 58527